Journal of Dairy Science · 1973 · 44 citations · 9 references
Life SciencesBiochemistryMolecular BiologyEnzymologyProtein BiochemistryProteomicsPeptide AnalysisPeptide ChemistryProtein AmidationProtein DegradationProteolytic EnzymesProteolytic ProcessingPeptidase ActivityProtease-catalyzed Peptide CleavageProteolytic ActivityProteolytic Enzyme ActivitySynthetic Peptide Characterization
The hexapeptide I-ILeu-Ser-Phe (NO2)-Nle-Ala-Leu-Ome is proposed as a reference for proteolytic activity determinations of chymosin (rennin). This peptide which is readily hydrolyzed by the enzyme contains a spectroscopic probe Phe (NO~) which facilitates routine determination of enzyme activity. Specific proteolytic activity has been measured for various purified and commercial enzyme preparations and compared to their clotting activity.
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Simplified Statistics for Small Numbers of Observations
Rochelle Dean, W. J. Dixon · Analytical Chemistry · 1951 · 937 citations
The purification and crystallization of rennin
N. J. Berridge · Biochemical Journal · 1945 · 121 citations · Full text
C Alais, G. Mocquot, Hs. Nitschmann et al. · Helvetica Chimica Acta · 1953 · 80 citations
Studies on the specificity of chymosin (rennin)
Marie‐Noëlle Raymond, J. Garnier, E. Bricas et al. · Biochimie · 1972 · 42 citations